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RNE_NEOYE
ID   RNE_NEOYE               Reviewed;         509 AA.
AC   Q1XDS6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Ribonuclease E/G-like protein;
DE            Short=RNase E/G-like protein;
DE            EC=3.1.26.-;
GN   Name=rne;
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in intercistronic processing of primary transcripts
CC       from chloroplast operons. The endonucleolytic activity of the enzyme
CC       depends on the number of phosphates at the 5' end, is inhibited by
CC       structured RNA, and preferentially cleaves A/U-rich sequences.
CC       {ECO:0000250|UniProtKB:F4IV66}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P21513};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000250|UniProtKB:F4IV66}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. {ECO:0000305}.
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DR   EMBL; AP006715; BAE92335.1; -; Genomic_DNA.
DR   RefSeq; YP_536892.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDS6; -.
DR   SMR; Q1XDS6; -.
DR   GeneID; 3978795; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR004659; RNase_E/G.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR30001; PTHR30001; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00757; RNaseEG; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   mRNA processing; Nuclease; Plastid; RNA-binding.
FT   CHAIN           1..509
FT                   /note="Ribonuclease E/G-like protein"
FT                   /id="PRO_0000277283"
FT   DOMAIN          35..117
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
SQ   SEQUENCE   509 AA;  58425 MW;  174FC39931AB5255 CRC64;
     MTNTIVISCL HNMAAILYCG QIQKLVVANA HYQVSDIYLG CVDKIFSGIN AAFINLGKNE
     YSGFIHISDT GPLKKKYYVN NITNILTIRQ KILVQIIKEP TLNKGPRLTA NITLSGRYIV
     LMPFSQSICI SRKIYDEDER HYLKSLAILI KPATMGLLFR PSAVGVDEEI ILSELKNLKE
     QWNFVQKSAI NSYSPVLLYK DEDIVKKVIR DFYNNNTNNI VIDSNLGLKQ LNYYIHTWHC
     NNSSTVPKIK LYSNNQCILD AFGINQAISR ALIPKVDLIL GGYMFIETLE AFTIIDVNSG
     SFNNSTSARE TVLKTNCSAA TEIAYQLQIR NITGVIIIDF IDMESQRDQL QLLEHFNKEL
     SLDDAKPQIV QLSELGLVEL TRRRQGKSLY ELISSDSNYF YFFTQSERSQ SLKRFDDRQQ
     KQQIFNKSWL SAEINTINKV FFQKSNLCRP ANFYLIRNLY IVKSSITYKQ NYLLTHRSKL
     IYSKEYSKVL PSSYYLASLN KNSNQEFLS
 
 
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